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Conserved domains on  [gi|1770169323|gb|QFU03795|]
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Bifunctional polymyxin resistance protein ArnA [Pseudoalteromonas sp. THAF3]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FMT_core super family cl00395
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ...
 7-149 2.89e-24

Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The proteins of this superfamily contain a formyltransferase domain that hydrolyzes the removal of a formyl group from its substrate as part of a multistep transfer mechanism, and this alignment model represents the catalytic core of the formyltransferase domain. This family includes the following known members; Glycinamide Ribonucleotide Transformylase (GART), Formyl-FH4 Hydrolase, Methionyl-tRNA Formyltransferase, ArnA, and 10-Formyltetrahydrofolate Dehydrogenase (FDH). Glycinamide Ribonucleotide Transformylase (GART) catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyl-FH4 Hydrolase catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to FH4 and formate. Methionyl-tRNA Formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA, which plays important role in translation initiation. ArnA is required for the modification of lipid A with 4-amino-4-deoxy-l-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. 10-formyltetrahydrofolate dehydrogenase (FDH) catalyzes the conversion of 10-formyltetrahydrofolate, a precursor for nucleotide biosynthesis, to tetrahydrofolate. Members of this family are multidomain proteins. The formyltransferase domain is located at the N-terminus of FDH, Methionyl-tRNA Formyltransferase and ArnA, and at the C-terminus of Formyl-FH4 Hydrolase. Prokaryotic Glycinamide Ribonucleotide Transformylase (GART) is a single domain protein while eukaryotic GART is a trifunctional protein that catalyzes the second, third and fifth steps in de novo purine biosynthesis.


The actual alignment was detected with superfamily member cd08369:

Pssm-ID: 444886 [Multi-domain]  Cd Length: 173  Bit Score: 94.28  E-value: 2.89e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770169323   7 AKKGDDASSSALSYLHDKGFDVEHHFGEWGDKLphsaAQWRGDIIISYLSRWIVPQALLDRANIAAINFHPAP-PEYPGI 85
Cdd:cd08369    33 DSPRGTAQLSLELVGGKVYLDSNINTPELLELL----KEFAPDLIVSINFRQIIPPEILKLPPGGAINIHPSLlPRYRGV 108

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1770169323  86 GCNNFALYNNEKTFGVTCHHMKAAVDTGEIIATKEFDLDASDNVESILKRAYDAQLALFQEVID 149
Cdd:cd08369   109 NPLAWAIINGEKETGVTVHYMDEGIDTGDIIAQEVIPISPDDTAGTLYQRLIELGPKLLKEALQ 172
 
Name Accession Description Interval E-value
FMT_core cd08369
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ...
 7-149 2.89e-24

Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The proteins of this superfamily contain a formyltransferase domain that hydrolyzes the removal of a formyl group from its substrate as part of a multistep transfer mechanism, and this alignment model represents the catalytic core of the formyltransferase domain. This family includes the following known members; Glycinamide Ribonucleotide Transformylase (GART), Formyl-FH4 Hydrolase, Methionyl-tRNA Formyltransferase, ArnA, and 10-Formyltetrahydrofolate Dehydrogenase (FDH). Glycinamide Ribonucleotide Transformylase (GART) catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyl-FH4 Hydrolase catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to FH4 and formate. Methionyl-tRNA Formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA, which plays important role in translation initiation. ArnA is required for the modification of lipid A with 4-amino-4-deoxy-l-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. 10-formyltetrahydrofolate dehydrogenase (FDH) catalyzes the conversion of 10-formyltetrahydrofolate, a precursor for nucleotide biosynthesis, to tetrahydrofolate. Members of this family are multidomain proteins. The formyltransferase domain is located at the N-terminus of FDH, Methionyl-tRNA Formyltransferase and ArnA, and at the C-terminus of Formyl-FH4 Hydrolase. Prokaryotic Glycinamide Ribonucleotide Transformylase (GART) is a single domain protein while eukaryotic GART is a trifunctional protein that catalyzes the second, third and fifth steps in de novo purine biosynthesis.


Pssm-ID: 187712 [Multi-domain]  Cd Length: 173  Bit Score: 94.28  E-value: 2.89e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770169323   7 AKKGDDASSSALSYLHDKGFDVEHHFGEWGDKLphsaAQWRGDIIISYLSRWIVPQALLDRANIAAINFHPAP-PEYPGI 85
Cdd:cd08369    33 DSPRGTAQLSLELVGGKVYLDSNINTPELLELL----KEFAPDLIVSINFRQIIPPEILKLPPGGAINIHPSLlPRYRGV 108

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1770169323  86 GCNNFALYNNEKTFGVTCHHMKAAVDTGEIIATKEFDLDASDNVESILKRAYDAQLALFQEVID 149
Cdd:cd08369   109 NPLAWAIINGEKETGVTVHYMDEGIDTGDIIAQEVIPISPDDTAGTLYQRLIELGPKLLKEALQ 172
Fmt COG0223
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
44-197 1.84e-18

Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 439993 [Multi-domain]  Cd Length: 308  Bit Score: 81.69  E-value: 1.84e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770169323  44 AQWRGDIIISYLSRWIVPQALLDRANIAAINFHPAP-PEYPG---IgcnNFALYNNEKTFGVTCHHMKAAVDTGEIIATK 119
Cdd:COG0223    75 RALNPDLIVVVAYGQILPKEVLDIPRLGCINLHASLlPRYRGaapI---QWAILNGDTETGVTIMQMDEGLDTGDILLQE 151

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1770169323 120 EFDLDASDNVESILKRAYDAQLALFQEVIDTFvKDGKfAVANKQWARKP-YTRKEFEELFIITPQMDADEVQRRVRAVS 197
Cdd:COG0223   152 EVPIGPDDTAGSLHDKLAELGAELLLETLDAL-EAGT-LTPTPQDESGAtYAPKISKEDGRIDWSRPAEEIHRLIRALN 228
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 59-148 9.85e-11

Formyl transferase; This family includes the following members. Glycinamide ribonucleotide transformylase catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyltetrahydrofolate deformylase produces formate from formyl- tetrahydrofolate. Methionyl-tRNA formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA. Inclusion of the following members is supported by PSI-blast. HOXX_BRAJA (P31907) contains a related domain of unknown function. PRTH_PORGI (P46071) contains a related domain of unknown function. Y09P_MYCTU (Q50721) contains a related domain of unknown function.


Pssm-ID: 395436 [Multi-domain]  Cd Length: 181  Bit Score: 58.46  E-value: 9.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770169323  59 IVPQALLDRANIAAINFHPA-PPEYPGIGCNNFALYNNEKTFGVTCHHMKAAVDTGEIIATKEFDLDASDNVESILKRAY 137
Cdd:pfam00551  91 ILPPEFLQAPPGGILNIHPSlLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDDTAETLYNRVA 170

                          90
                  ....*....|.
gi 1770169323 138 DAQLALFQEVI 148
Cdd:pfam00551 171 DLEHKALPRVL 181
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
 34-155 1.26e-10

phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model describes phosphoribosylglycinamide formyltransferase (GAR transformylase), one of several proteins in formyl_transf (pfam00551). This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. PurT, a different GAR transformylase, uses ATP and formate rather than formyl tetrahydrofolate. Experimental proof includes complementation of E. coli purN mutants by orthologs from vertebrates (where it is a domain of a multifunctional protein), Bacillus subtilis, and Arabidopsis. No archaeal example was detected. In phylogenetic analyses, the member from Saccharomyces cerevisiae shows a long branch length but membership in the family, while the formyltetrahydrofolate deformylases form a closely related outgroup. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 161973 [Multi-domain]  Cd Length: 190  Bit Score: 58.54  E-value: 1.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770169323  34 EWGDKLPHSAAQWRGDIIIsyLSRW--IVPQALLDRANIAAINFHPA-PPEYPGIGCNNFALYNNEKTFGVTCHHMKAAV 110
Cdd:TIGR00639  66 AFDQAIIEELRAHEVDLVV--LAGFmrILGPTFLSRFAGRILNIHPSlLPAFPGLHAVEQALEAGVKESGCTVHYVDEEV 143

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1770169323 111 DTGEIIATKEFDLDASDNVESILKRAYDAQLALFQEVIDTFVKDG 155
Cdd:TIGR00639 144 DTGPIIAQAKVPILPEDTEETLEQRIHKQEHRIYPLAIAWFAQGR 188
PRK08125 PRK08125
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ...
 27-204 2.79e-10

bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ArnA;


Pssm-ID: 236156 [Multi-domain]  Cd Length: 660  Bit Score: 59.23  E-value: 2.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770169323  27 DVEHHFgeWGDKLphsaAQWRGDIIISYLSRWIVPQALLDRANIAAINFHPAP-PEYPGIGCNNFALYNNEKTFGVTCHH 105
Cdd:PRK08125   61 DVNHPL--WVERI----RELAPDVIFSFYYRNLLSDEILQLAPAGAFNLHGSLlPKYRGRAPLNWVLVNGETETGVTLHR 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770169323 106 MKAAVDTGEIIATKEFDLDASDNVESILKRAYDAQLALFQEVIDTfVKDGKFAVANKQWARKPYTRKEFEELFIITPQMD 185
Cdd:PRK08125  135 MVKRADAGAIVAQQRVAIAPDDTALTLHHKLCHAARQLLEQTLPA-IKHGNIPEIPQDESQATYFGRRTPADGLIDWHKP 213

                         170
                  ....*....|....*....
gi 1770169323 186 ADEVQRRVRAVSfrqyQPY 204
Cdd:PRK08125  214 ASTLHNLVRAVT----DPW 228
 
Name Accession Description Interval E-value
FMT_core cd08369
Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The ...
 7-149 2.89e-24

Formyltransferase, catalytic core domain; Formyltransferase, catalytic core domain. The proteins of this superfamily contain a formyltransferase domain that hydrolyzes the removal of a formyl group from its substrate as part of a multistep transfer mechanism, and this alignment model represents the catalytic core of the formyltransferase domain. This family includes the following known members; Glycinamide Ribonucleotide Transformylase (GART), Formyl-FH4 Hydrolase, Methionyl-tRNA Formyltransferase, ArnA, and 10-Formyltetrahydrofolate Dehydrogenase (FDH). Glycinamide Ribonucleotide Transformylase (GART) catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyl-FH4 Hydrolase catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to FH4 and formate. Methionyl-tRNA Formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA, which plays important role in translation initiation. ArnA is required for the modification of lipid A with 4-amino-4-deoxy-l-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. 10-formyltetrahydrofolate dehydrogenase (FDH) catalyzes the conversion of 10-formyltetrahydrofolate, a precursor for nucleotide biosynthesis, to tetrahydrofolate. Members of this family are multidomain proteins. The formyltransferase domain is located at the N-terminus of FDH, Methionyl-tRNA Formyltransferase and ArnA, and at the C-terminus of Formyl-FH4 Hydrolase. Prokaryotic Glycinamide Ribonucleotide Transformylase (GART) is a single domain protein while eukaryotic GART is a trifunctional protein that catalyzes the second, third and fifth steps in de novo purine biosynthesis.


Pssm-ID: 187712 [Multi-domain]  Cd Length: 173  Bit Score: 94.28  E-value: 2.89e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770169323   7 AKKGDDASSSALSYLHDKGFDVEHHFGEWGDKLphsaAQWRGDIIISYLSRWIVPQALLDRANIAAINFHPAP-PEYPGI 85
Cdd:cd08369    33 DSPRGTAQLSLELVGGKVYLDSNINTPELLELL----KEFAPDLIVSINFRQIIPPEILKLPPGGAINIHPSLlPRYRGV 108

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1770169323  86 GCNNFALYNNEKTFGVTCHHMKAAVDTGEIIATKEFDLDASDNVESILKRAYDAQLALFQEVID 149
Cdd:cd08369   109 NPLAWAIINGEKETGVTVHYMDEGIDTGDIIAQEVIPISPDDTAGTLYQRLIELGPKLLKEALQ 172
FMT_core_NRPS_like cd08649
N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins ...
 34-149 2.57e-20

N-terminal formyl transferase catalytic core domain of NRPS_like proteins, one of the proteins involved in the synthesis of Oxazolomycin; This family represents the N-terminal formyl transferase catalytic core domain present in a subgroup of non-ribosomal peptide synthetases. In Streptomyces albus a member of this family has been shown to be involved in the synthesis of oxazolomycin (OZM). OZM is a hybrid peptide-polyketide antibiotic and exhibits potent antitumor and antiviral activities. It is a multi-domain protein consisting of a formyl transferase domain, a Flavin-utilizing monoxygenase domain, a LuxE domain functioning as an acyl protein synthetase and a pp-binding domain, which may function as an acyl carrier. It shows sequence similarity with other peptide-polyketide biosynthesis proteins.


Pssm-ID: 187718 [Multi-domain]  Cd Length: 166  Bit Score: 83.85  E-value: 2.57e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770169323  34 EWGDKLPHSAAQWRGDIIISYLSRWIVPQALLDRANIAAINFHPAP-PEYPGIGCNNFALYNNEKTFGVTCHHMKAAVDT 112
Cdd:cd08649    48 EPGEALEELLSDEPFDWLFSIVNLRILPSEVLALPRKGAINFHDGPlPRYAGLNATSWALLAGETRHGVTWHRIEEGVDA 127

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1770169323 113 GEIIATKEFDLDASDNVESILKRAYDAQLALFQEVID 149
Cdd:cd08649   128 GDILVQRPFDIAPDDTALSLNLKCYEAGIEGFGELID 164
FMT_core_like_6 cd08820
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 49-148 2.64e-19

Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.


Pssm-ID: 187722 [Multi-domain]  Cd Length: 173  Bit Score: 81.33  E-value: 2.64e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770169323  49 DIIISYLSRWIVPQALLDRANIAAINFHPAP-PEYPGIGCNNFALYNNEKTFGVTCHHMKAAVDTGEIIATKEFDLDASD 127
Cdd:cd08820    71 DILISVQYHWILPGSILEKAKEIAFNLHNAPlPEYRGCNQFSHAILNGDDQFGTTIHWMAEGIDSGDIIFEKRFPIPSDC 150

                          90       100
                  ....*....|....*....|.
gi 1770169323 128 NVESILKRAYDAQLALFQEVI 148
Cdd:cd08820   151 TVISLYILAHYAAIALFGEHI 171
Fmt COG0223
Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];
44-197 1.84e-18

Methionyl-tRNA formyltransferase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 439993 [Multi-domain]  Cd Length: 308  Bit Score: 81.69  E-value: 1.84e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770169323  44 AQWRGDIIISYLSRWIVPQALLDRANIAAINFHPAP-PEYPG---IgcnNFALYNNEKTFGVTCHHMKAAVDTGEIIATK 119
Cdd:COG0223    75 RALNPDLIVVVAYGQILPKEVLDIPRLGCINLHASLlPRYRGaapI---QWAILNGDTETGVTIMQMDEGLDTGDILLQE 151

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1770169323 120 EFDLDASDNVESILKRAYDAQLALFQEVIDTFvKDGKfAVANKQWARKP-YTRKEFEELFIITPQMDADEVQRRVRAVS 197
Cdd:COG0223   152 EVPIGPDDTAGSLHDKLAELGAELLLETLDAL-EAGT-LTPTPQDESGAtYAPKISKEDGRIDWSRPAEEIHRLIRALN 228
FMT_core_like_3 cd08653
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 44-151 1.76e-15

Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.


Pssm-ID: 187721 [Multi-domain]  Cd Length: 152  Bit Score: 70.70  E-value: 1.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770169323  44 AQWRGDIIISYLSRwIVPQALLDRANIAAINFHP-APPEYPGIGCNNFALYNNE-KTFGVTCHHMKAAVDTGEIIATKEF 121
Cdd:cd08653    44 RALAPDVVSVYGCG-IIKDALLAIPPLGVLNLHGgILPDYRGVHTGFWALANGDpDNVGVTVHLVDAGIDTGDVLAQARP 122

                          90       100       110
                  ....*....|....*....|....*....|
gi 1770169323 122 DLDASDNVESILKRAYDAQLALFQEVIDTF 151
Cdd:cd08653   123 PLAAGDTLLSLYLRLYRAGVELMVEAIADL 152
Formyl_trans_N pfam00551
Formyl transferase; This family includes the following members. Glycinamide ribonucleotide ...
 59-148 9.85e-11

Formyl transferase; This family includes the following members. Glycinamide ribonucleotide transformylase catalyzes the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyltetrahydrofolate deformylase produces formate from formyl- tetrahydrofolate. Methionyl-tRNA formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA. Inclusion of the following members is supported by PSI-blast. HOXX_BRAJA (P31907) contains a related domain of unknown function. PRTH_PORGI (P46071) contains a related domain of unknown function. Y09P_MYCTU (Q50721) contains a related domain of unknown function.


Pssm-ID: 395436 [Multi-domain]  Cd Length: 181  Bit Score: 58.46  E-value: 9.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770169323  59 IVPQALLDRANIAAINFHPA-PPEYPGIGCNNFALYNNEKTFGVTCHHMKAAVDTGEIIATKEFDLDASDNVESILKRAY 137
Cdd:pfam00551  91 ILPPEFLQAPPGGILNIHPSlLPRFRGAAPIQRALEAGDKETGVTIHFVDEGLDTGPILAQKAVPILPDDTAETLYNRVA 170

                          90
                  ....*....|.
gi 1770169323 138 DAQLALFQEVI 148
Cdd:pfam00551 171 DLEHKALPRVL 181
PurN TIGR00639
phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model ...
 34-155 1.26e-10

phosphoribosylglycinamide formyltransferase, formyltetrahydrofolate-dependent; This model describes phosphoribosylglycinamide formyltransferase (GAR transformylase), one of several proteins in formyl_transf (pfam00551). This enzyme uses formyl tetrahydrofolate as a formyl group donor to produce 5'-phosphoribosyl-N-formylglycinamide. PurT, a different GAR transformylase, uses ATP and formate rather than formyl tetrahydrofolate. Experimental proof includes complementation of E. coli purN mutants by orthologs from vertebrates (where it is a domain of a multifunctional protein), Bacillus subtilis, and Arabidopsis. No archaeal example was detected. In phylogenetic analyses, the member from Saccharomyces cerevisiae shows a long branch length but membership in the family, while the formyltetrahydrofolate deformylases form a closely related outgroup. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 161973 [Multi-domain]  Cd Length: 190  Bit Score: 58.54  E-value: 1.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770169323  34 EWGDKLPHSAAQWRGDIIIsyLSRW--IVPQALLDRANIAAINFHPA-PPEYPGIGCNNFALYNNEKTFGVTCHHMKAAV 110
Cdd:TIGR00639  66 AFDQAIIEELRAHEVDLVV--LAGFmrILGPTFLSRFAGRILNIHPSlLPAFPGLHAVEQALEAGVKESGCTVHYVDEEV 143

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1770169323 111 DTGEIIATKEFDLDASDNVESILKRAYDAQLALFQEVIDTFVKDG 155
Cdd:TIGR00639 144 DTGPIIAQAKVPILPEDTEETLEQRIHKQEHRIYPLAIAWFAQGR 188
FMT_core_ArnA_N cd08644
ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for ...
 34-139 2.68e-10

ArnA, N-terminal formyltransferase domain; ArnA_N: ArnA is a bifunctional enzyme required for the modification of lipid A with 4-amino-4-deoxy-L-arabinose (Ara4N) that leads to resistance to cationic antimicrobial peptides (CAMPs) and clinical antimicrobials such as polymyxin. The C-terminal dehydrogenase domain of ArnA catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O), while the N-terminal formyltransferase domain of ArnA catalyzes the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). This domain family represents the catalytic core of the N-terminal formyltransferase domain. The formyltransferase also contains a smaller C-terminal domain the may be involved in substrate binding. ArnA forms a hexameric structure, in which the dehydrogenase domains are arranged at the center of the particle with the transformylase domains on the outside of the particle.


Pssm-ID: 187713 [Multi-domain]  Cd Length: 203  Bit Score: 57.74  E-value: 2.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770169323  34 EWGDKLphsaAQWRGDIIISYLSRWIVPQALLDRANIAAINFHPAP-PEYPGIGCNNFALYNNEKTFGVTCHHMKAAVDT 112
Cdd:cd08644    66 EWVERL----RALKPDLIFSFYYRHMISEDILEIARLGAFNLHGSLlPKYRGRAPLNWALINGETETGVTLHRMTKKPDA 141

                          90       100
                  ....*....|....*....|....*..
gi 1770169323 113 GEIIATKEFDLDASDNVESILKRAYDA 139
Cdd:cd08644   142 GAIVDQEKVPILPDDTAKSLFHKLCVA 168
PRK08125 PRK08125
bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ...
 27-204 2.79e-10

bifunctional UDP-4-amino-4-deoxy-L-arabinose formyltransferase/UDP-glucuronic acid oxidase ArnA;


Pssm-ID: 236156 [Multi-domain]  Cd Length: 660  Bit Score: 59.23  E-value: 2.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770169323  27 DVEHHFgeWGDKLphsaAQWRGDIIISYLSRWIVPQALLDRANIAAINFHPAP-PEYPGIGCNNFALYNNEKTFGVTCHH 105
Cdd:PRK08125   61 DVNHPL--WVERI----RELAPDVIFSFYYRNLLSDEILQLAPAGAFNLHGSLlPKYRGRAPLNWVLVNGETETGVTLHR 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770169323 106 MKAAVDTGEIIATKEFDLDASDNVESILKRAYDAQLALFQEVIDTfVKDGKFAVANKQWARKPYTRKEFEELFIITPQMD 185
Cdd:PRK08125  135 MVKRADAGAIVAQQRVAIAPDDTALTLHHKLCHAARQLLEQTLPA-IKHGNIPEIPQDESQATYFGRRTPADGLIDWHKP 213

                         170
                  ....*....|....*....
gi 1770169323 186 ADEVQRRVRAVSfrqyQPY 204
Cdd:PRK08125  214 ASTLHNLVRAVT----DPW 228
FMT_core_like_5 cd08823
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 58-128 8.55e-10

Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.


Pssm-ID: 187725 [Multi-domain]  Cd Length: 177  Bit Score: 55.91  E-value: 8.55e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1770169323  58 WIVPQALLDRANIAAINFHPAP-PEYPGIGCNNFALYNNEKTFGVTCHHMKAAVDTGEIIATKEFDLDASDN 128
Cdd:cd08823    82 YRIPQHILDLPPLGFYNLHPGLlPAYRGPDPLFWQIRNQEQETAITVHKMTAEIDRGPIVLEQFTPIHPDDT 153
PRK07579 PRK07579
dTDP-4-amino-4,6-dideoxyglucose formyltransferase;
47-209 3.42e-09

dTDP-4-amino-4,6-dideoxyglucose formyltransferase;


Pssm-ID: 236058 [Multi-domain]  Cd Length: 245  Bit Score: 55.29  E-value: 3.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770169323  47 RGDIIISYLSRWIVPQALLDraNIAAINFHPA-PPEYPGIGCNNFALYNNEKtFGVTCHHMKAAVDTGEIIATKEFDLDA 125
Cdd:PRK07579   65 RYDLVLSFHCKQRFPAKLVN--GVRCINIHPGfNPYNRGWFPQVFSIINGLK-IGATIHEMDEQLDHGPIIAQREVEIES 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770169323 126 SDNVESILKRAYDAQLALFQEVIDTfVKDGKFAVANKQWARKPYTRKEFEELFiitpQMDADEVQ------RRVRAVSFR 199
Cdd:PRK07579  142 WDSSGSVYARVMDIERELVLEHFDA-IRDGSYTAKKPATEGNLNSKKDFKQLR----EIDLDERGtfrhfiNRLRALTHD 216

                         170
                  ....*....|..
gi 1770169323 200 QYQP--YIKLHG 209
Cdd:PRK07579  217 DYKNayFVDESG 228
FMT_core_Met-tRNA-FMT_N cd08646
Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA ...
 59-135 7.10e-09

Methionyl-tRNA formyltransferase, N-terminal hydrolase domain; Methionyl-tRNA formyltransferase (Met-tRNA-FMT), N-terminal formyltransferase domain. Met-tRNA-FMT transfers a formyl group from N-10 formyltetrahydrofolate to the amino terminal end of a methionyl-aminoacyl-tRNA acyl moiety, yielding formyl-Met-tRNA. Formyl-Met-tRNA plays essential role in protein translation initiation by forming complex with IF2. The formyl group plays a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and by impairing its binding to EFTU-GTP. The N-terminal domain contains a Rossmann fold and it is the catalytic domain of the enzyme.


Pssm-ID: 187715 [Multi-domain]  Cd Length: 204  Bit Score: 53.60  E-value: 7.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770169323  59 IVPQALLDRANIAAINFHP---------APPEYpgigcnnfALYNNEKTFGVTCHHMKAAVDTGEIIATKEFDLDASDNV 129
Cdd:cd08646    90 ILPKEILDLPPYGCINVHPsllpkyrgaAPIQR--------AILNGDKETGVTIMKMDEGLDTGDILAQEEVPIDPDDTA 161


                  ....*.
gi 1770169323 130 ESILKR 135
Cdd:cd08646   162 GELLDK 167
FMT_core_HypX_N cd08650
HypX protein, N-terminal hydrolase domain; The family represents the N-terminal hydrolase ...
 1-151 4.68e-07

HypX protein, N-terminal hydrolase domain; The family represents the N-terminal hydrolase domain of HypX protein. HypX is involved in the maturation process of active [NiFe] hydrogenase. [NiFe] hydrogenases function in H2 metabolism in a variety of microorganisms, enabling them to use H2 as a source of reducing equivalent under aerobic and anaerobic conditions. [NiFe] hydrogenases consist of a large and a small subunit. The large subunit contains [NiFe] active site, which is synthesized as a precursor without the [NiFe] active site. This precursor then undergoes a complex post-translational maturation process that requires the presence of a number of accessory proteins. HypX has been shown to be involved in this maturation process and have been proposed to participate in the generation and transport of the CO and CN ligands. However, HypX is not present in all hydrogen-metabolizing bacteria. Furthermore, hypX deletion mutants have a reduced but detectable level of hydrogenase activity. Thus, HypX might not be a determining factor in the matur ation process. Members of this group have an N-terminal formyl transferase domain and a C-terminal enoyl-CoA hydratase/isomerase domain.


Pssm-ID: 187719 [Multi-domain]  Cd Length: 151  Bit Score: 47.61  E-value: 4.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770169323   1 MKVLFLAKKGDDASSSALSYLHDKGFDVEHHFGEWGDKLPHSAAQWRGDIIIS-YLSRWIvPQALLDraNIAAINFHPAP 79
Cdd:cd08650     1 MKILLLCSAFNSLTQRAFLELRERGHEVSVEYALSDDEMREAVALFAPDLIICpFLKKRI-PEEIWS--NYPCLIVHPGI 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1770169323  80 PEYPGIGCNNFALYNNEKTFGVTCHHMKAAVDTGEIIATKEFDLDASDNVESILKR-AYDAQLALFQEVIDTF 151
Cdd:cd08650    78 VGDRGPSSLDWAILEGEKEWGVTVLQAVEEMDAGPIWATRNFPLRRAATKSSLYRGeVTDAAVKAVLEAVENF 150
PRK06988 PRK06988
formyltransferase;
47-142 5.43e-07

formyltransferase;


Pssm-ID: 235902 [Multi-domain]  Cd Length: 312  Bit Score: 48.92  E-value: 5.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770169323  47 RGDIIISYLSRWIVPQALLDRANIAAINFHPA-PPEYPGIGCNNFALYNNEKTFGVTCHHMKAAVDTGEII--------- 116
Cdd:PRK06988   77 APDFIFSFYYRHMIPVDLLALAPRGAYNMHGSlLPKYRGRVPVNWAVLNGETETGATLHEMVAKPDAGAIVdqtavpilp 156

                          90       100
                  ....*....|....*....|....*....
gi 1770169323 117 ---ATKEFDlDASDNVESILKRAYDAQLA 142
Cdd:PRK06988  157 ddtAAQVFD-KVTVAAEQTLWRVLPALLA 184
FMT_core_like_4 cd08651
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 52-154 3.64e-06

Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.


Pssm-ID: 187720 [Multi-domain]  Cd Length: 180  Bit Score: 45.72  E-value: 3.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770169323  52 ISYLSRW--IVPQALLDRANIAAINFHPAP-PEYPGIGCNNFALYNNEKTFGVTCHHMKAAVDTGEIIATKEFDLDASDN 128
Cdd:cd08651    78 IIFVFGWsqLLKPEILAIPRLGVIGFHPTKlPKNRGRAPIPWAILLGLKETASTFFWMDEGADSGDILSQEPFPIDKDDT 157

                          90       100
                  ....*....|....*....|....*.
gi 1770169323 129 VESIlkraYDAQLALFQEVIDTFVKD 154
Cdd:cd08651   158 ANSL----YDKIMEAAKQQIDKFLPR 179
PurN COG0299
Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and ...
 59-135 2.46e-05

Folate-dependent phosphoribosylglycinamide formyltransferase PurN [Nucleotide transport and metabolism]; Folate-dependent phosphoribosylglycinamide formyltransferase PurN is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440068 [Multi-domain]  Cd Length: 202  Bit Score: 43.48  E-value: 2.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770169323  59 IVPQALLDRANIAAINFHPA-PPEYPG---IGCnnfALYNNEKTFGVTCHHMKAAVDTGEIIATKEFDLDASDNVESILK 134
Cdd:COG0299    92 ILTPEFVRAFPGRIINIHPSlLPAFPGlhaHRQ---ALEAGVKVTGCTVHFVDEEVDTGPIIAQAAVPVLPDDTEETLAA 168


                  .
gi 1770169323 135 R 135
Cdd:COG0299   169 R 169
FMT_core_like_2 cd08822
Formyl transferase catalytic core domain found in a group of proteins with unknown functions; ...
 49-155 4.43e-03

Formyl transferase catalytic core domain found in a group of proteins with unknown functions; Formyl transferase catalytic core domain found in a group of proteins with unknown functions. Formyl transferase catalyzes the transfer of one-carbon groups, specifically the formyl- or hydroxymethyl- group. This domain contains a Rossmann fold and it is the catalytic domain of the enzyme.


Pssm-ID: 187724 [Multi-domain]  Cd Length: 192  Bit Score: 36.67  E-value: 4.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770169323  49 DIIISYLSRWIVPQALLDRANIAAINFHPAP-PEYPGIGCNNFALYNNEKTFGVTCHHMKAAVDTGEIIATKEFDLDASD 127
Cdd:cd08822    68 DLIVAAHCHAFISAKTRARARLGAIGYHPSLlPRHRGRDAVEWTIRMRDPITGGTVYHLDDGVDGGPIAAQDWCHVRPGD 147

                          90       100
                  ....*....|....*....|....*....
gi 1770169323 128 NVESILKRA-YDAQLALFQEVIDTFVKDG 155
Cdd:cd08822   148 TAAELWRRAlAPMGVKLLTQVIDALLRGG 176
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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